@article { ISI:000325949600005,
	title = {Kinetics and thermodynamics of glycans and glycoproteins binding to holothuria scabra lectin: a fluorescence and surface plasmon resonance spectroscopic study},
	journal = {Journal of Fluorescence},
	volume = {23},
	number = {6},
	year = {2013},
	month = {NOV},
	pages = {1147-1155},
	publisher = {SPRINGER/PLENUM PUBLISHERS},
	address = {233 SPRING ST, NEW YORK, NY 10013 USA},
	abstract = {<p>Holothuria scabra produces a monomeric lectin (HSL) of 182 kDa. HSL showed strong antibacterial activity and induced bacterial agglutination under in vitro conditions, indicating its role in animals{\textquoteright} innate immune responses. Very few lectins have been reported from echinoderms and none of these lectins have been explored in detail for their sugar-binding kinetics. Affinity, kinetics and thermodynamic analysis of glycans and glycoproteins binding to HSL were studied by fluorescence and surface plasmon resonance spectroscopy. Lectin binds with higher affinity to O-linked than N-linked asialo glycans, and the affinities were relatively higher than that for sialated glycans and glycoproteins. T-antigen alpha-methyl glycoside was the most potent ligand having the highest affinity (Ka 8.32 x10(7) M-1). Thermodynamic and kinetic analysis indicated that the binding of galactosyl Tn-antigen and asialo glycans is accompanied by an enthalpic contribution in addition to higher association rate coupled by low activation energy for the association process. Presence of sialic acid or protein matrix inhibits binding. Higher affinity of HSL for O-glycans than N-glycans had biological implications; since HSL specifically recognizes bacteria, which have mucin or O-glycan cognate on their cell surfaces and play a major role in animal innate immunity. Since, HSL had higher affinity to T-antigen, makes it a useful tool for cancer diagnostic purpose.</p>},
	keywords = {Holothuria scabra, Kinetic analysis, Lectin, Surface plasmon resonance spectroscopy, Thermodynamic properties},
	issn = {1053-0509},
	doi = {10.1007/s10895-013-1244-4},
	author = {Gowda, Nagaraj M. and Gaikwad, Sushama M. and Khan, Mohammad Islam}
}
@article {45551,
	title = {Investigation of structural and saccharide binding transitions of Bauhinia purpurea and Wisteria floribunda lectins},
	journal = {Archives of Biochemistry and Biophysics},
	volume = {662},
	year = {2019},
	month = {FEB },
	pages = {134-142},
	type = {Article},
	abstract = {<p>Two novel medicinally important legume lectins from Bauhinia purpurea (BPL) and Wisteria floribunda (WFL) possessing extended sugar binding site were investigated for functional and conformational transitions using biochemical and biophysical techniques as well as bioinformatical tools. Homology model of BPL was constructed using the Schrodinger suite and docked with N-acetyl galactosamine and T-antigen disaccharide (Gal beta 1-3GalNAc alpha O-Me). The longer loop D in the structure of WFL compared to that in BPL was found to be responsible for its specificity to LacdiNac (beta-D-GalNAc-[1 -\&gt; 4]-DGlcNAc) over Gal beta 1-3GalNAc. BPL remained functionally stable up to 40 degrees C whereas WFL remained stable upto 70 degrees C indicating the strength of the sugar binding site geometry. Both the lectins showed intense but non-specific secondary structure in the range of 65-90 degrees C. WFL showed rapid aggregation above 80 degrees C as indicated by light scattering intensity. The lectins showed simultaneous dissociation and multistate unfolding in the vicinity of GdnHCl. At pH 1.0, both the lectins exhibited molten globule like structures, which were characterized further and were found to respond in a different way towards denaturants. The results have provided valuable insights into the molecular basis of the activity and stability of the two lectins.</p>},
	keywords = {Conformation, Homology model, Lectin, Molten globule, saccharide binding, Thermal aggregation},
	issn = {0003-9861},
	doi = {10.1016/j.abb.2018.12.003},
	author = {Agrawal, Sanskruthi B. and Ghosh, Deepanjan and Gaikwad, Sushama M.}
}
